Soultanas P, Wigley D B
Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
Curr Opin Struct Biol. 2000 Feb;10(1):124-8. doi: 10.1016/s0959-440x(99)00059-7.
Recently determined crystal structures of PcrA helicase complexed with a DNA substrate have revealed details of the helicase mechanism. PcrA and UvrD helicases have been shown to be functional as monomers, challenging previous suggestions that all helicases are required to be oligomeric. Crystal structures of the hexameric helicases RepA and T7 gene 4 explain the formation of hexameric assemblies from identical monomers with RecA-like folds, but their molecular mechanism remains elusive.
最近确定的与DNA底物复合的PcrA解旋酶晶体结构揭示了解旋酶机制的细节。已证明PcrA和解旋酶UvrD作为单体发挥功能，这对先前认为所有解旋酶都需要形成寡聚体的观点提出了挑战。六聚体解旋酶RepA和T7基因4的晶体结构解释了具有RecA样折叠的相同单体如何形成六聚体组装体，但其分子机制仍然难以捉摸。
